IMMOBILIZATION OF POTATO-TUBER LIPOXYGENASE ON OXIRANE ACRYLIC BEADS

In this study, Lipoxygenase from potato tuber has been purified by a m ethod involving hydrophobic chromatography and the purified enzyme imm obilized by covalent coupling to oxirane acrylic beads. The immobilize d lipoxygenase exhibited increased long-term stability without a signi ficant modification of the kinetic parameters. The comparative study o n the effects of inhibitors such as dithizone, NDGA, phenidone, and be ta-mercaptoethanol on the free and immobilized enzyme highlighted the importance of the lipoxygenase-support interaction, concluding that th e immobilization process could cause the protection of the iron atom i n the enzyme. The enzymatic specificity was maintained for the immobil ized lipoxygenase, and their stability increased as compared to the fr ee enzyme, making it feasible to use the enzyme in a multistep reactio n to produce large quantities of leukotriene A(4) or other related com pounds of interest in the chemical industry and medicine.